Several salt bridges observed in protein X-ray crystallographic structures showed a consistent pattern of a carboxylate, situated near the face of an aromatic ring, forming a bond to an arginine residue of a ligand. To determine the driving force for these complexes, H-1 NMR or potentiometric binding titrations were performed on solutions containing N-acetyl arginine methyl ester, N-acetyl lysine methyl ester, guanidinium chloride, or KCl and one member of a series of diacidic templates, which had aromatic or aliphatic groups placed below their carboxylates. Only templates having an aromatic ring were able to form a salt bridge in water. Although most of the obvious interactions, such as ionic and cation-pi, and ion desolvation are important factors, association of an amino acid in water required the presence of the entire amino acid. This result suggests that the interaction between the aliphatic portion of an amino acid and an aromatic ring of a template is an important component of complexation. Aromatic templates also transported N-acetyl arginine methyl ester from water to 1-octanol. The results of the transport studies are discussed in terms of potential intermediate states that could lower some of the activation barriers of protein folding.